ID   PTH_ACTP2               Reviewed;         194 AA.
AC   A3MYA5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   10-JUN-2026, entry version 100.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE            Short=Pth {ECO:0000255|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN   Name=pth {ECO:0000255|HAMAP-Rule:MF_00083};
GN   OrderedLocusNames=APL_0033;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
CC   -!- FUNCTION: Hydrolyzes ribosome-free peptidyl-tRNAs (with 1 or more amino
CC       acids incorporated), which drop off the ribosome during protein
CC       synthesis, or as a result of ribosome stalling. {ECO:0000255|HAMAP-
CC       Rule:MF_00083}.
CC   -!- FUNCTION: Catalyzes the release of premature peptidyl moieties from
CC       peptidyl-tRNA molecules trapped in stalled 50S ribosomal subunits, and
CC       thus maintains levels of free tRNAs and 50S ribosomes.
CC       {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = an N-acyl-L-amino
CC         acid + a tRNA + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC         Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC         EC=3.1.1.29; Evidence={ECO:0000255|HAMAP-Rule:MF_00083};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00083}.
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DR   EMBL; CP000569; ABN73141.1; -; Genomic_DNA.
DR   RefSeq; WP_005595643.1; NC_009053.1.
DR   AlphaFoldDB; A3MYA5; -.
DR   SMR; A3MYA5; -.
DR   STRING; 416269.APL_0033; -.
DR   EnsemblBacteria; ABN73141; ABN73141; APL_0033.
DR   GeneID; 48598174; -.
DR   KEGG; apl:APL_0033; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_3_1_6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:peptidyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR   GO; GO:0072344; P:rescue of stalled cytosolic ribosome; IEA:UniProtKB-UniRule.
DR   CDD; cd00462; PTH; 1.
DR   FunFam; 3.40.50.1470:FF:000001; Peptidyl-tRNA hydrolase; 1.
DR   Gene3D; 3.40.50.1470; Peptidyl-tRNA hydrolase; 1.
DR   HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR   NCBIfam; TIGR00447; pth; 1.
DR   PANTHER; PTHR17224; PEPTIDYL-TRNA HYDROLASE; 1.
DR   PANTHER; PTHR17224:SF1; PEPTIDYL-TRNA HYDROLASE; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; Peptidyl-tRNA hydrolase-like; 1.
DR   PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; RNA-binding; tRNA-binding.
FT   CHAIN           1..194
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_1000010556"
FT   ACT_SITE        22
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   BINDING         17
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   BINDING         68
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   BINDING         70
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   BINDING         116
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   SITE            12
FT                   /note="Discriminates between blocked and unblocked
FT                   aminoacyl-tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   SITE            95
FT                   /note="Stabilizes the basic form of H active site to accept
FT                   a proton"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
SQ   SEQUENCE   194 AA;  20825 MW;  9401F214B85C2DD9 CRC64;
     MSQIKLIVGL ANPGTKYEDT RHNAGEWLIN EIARQFNVSL KEEAKFFGKV AKINAAGGEV
     RLLVPTTFMN LSGKAVGALA NFYRIKPEEI LVAHDELDLP PGVAKIKQGG GHGGHNGLKD
     IIASLGNSNN FYRVRIGIGH PGSKELVAGY VLGKPSPQDQ EKINAAVDEA GRCVDLLLKD
     GITKATNRLN AFKA
//